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EFFECT OF LEUCINE-PROTEIN HIGH-CARBOHYDRATE POST-EXERCISE NUTRITION ON SUBSEQUENT
PERFORMANCE AND THE PROTEIN REGULATED GENOMIC AND SIGNALLING EVENTS GOVERNING ADAPTIVE
REMODELLING
A Thesis
Presented in partial fulfilment of the requirements
For the degree of Doctor of Philosophy
In
Nutritional Science
Massey University,
Albany,
New Zealand.
Jasmine Sarah Thomson
2010
i
DOCTOR OF PHILOSOPHY Massey University
(Nutritional Science) Auckland, New Zealand
TITLE: Effect of leucine-protein high-carbohydrate post-exercise
nutrition on subsequent performance and the protein regulated genomic and
signalling events governing adaptive remodelling
AUTHOR: Jasmine S. Thomson, BSc, MSc
SUPERVISOR: Dr. David S. Rowlands
CO-SUPERVISORS: Assoc. Prof. Welma Stonehouse, Dr. Ajmol Ali
NUMBER OF PAGES: xxiii; 354
ii
ABSTRACT Recovery from prolonged endurance exercise requires fuel replenishment
and ultrastructure repair to restore cellular homeostasis; and improvement
requires adaptive remodelling. Timing nutrient intake to closely follow
exercise may be advantageous to recovery and subsequent performance by
facilitating the adaptive processes stimulated by exercise. The objective of
this research was to firstly determine if leucine-enriched protein feeding after
hard training improved subsequent performance, and secondly to explore the
candidate means by which protein-rich post-exercise nutrition mediates
recovery, primarily transcriptomic and signalling mechanisms.
Study 1 Ten male cyclists ingested leucine-enriched protein-carbohydrate
(0.1/0.4/1.2/0.2 g·kg-1·h-1 leucine/protein/carbohydrate/fat) or isocaloric high-
carbohydrate control (0.06/1.6/0.2 g·kg-1·h-1) meals following 2-2.5 h high-
intensity interval training on 3 consecutive days. Cyclists performed a repeat-
sprint performance test 39 h after training, and markers of physiological
recovery and mood state were examined. Study 2 Eight male cyclists
ingested protein (0.4/1.2/0.2 g·kg-1·h-1 protein/carbohydrate/fat) or isocaloric
high-carbohydrate control (0.03/1.6/0.2 g·kg-1·h-1) beverages following a
single 1.75 h high-intensity interval cycling bout. Muscle tissue samples were
collected from the vastus lateralis before exercise, 3-h and 48-h post-
exercise. The transcriptome response was assessed by Illumina microarray,
candidate gene expression by real time RT-PCR; and phospho-protein
signalling by Western blot.
Leucine-enriched feeding increased mean sprint power by 2.5% (99%
confidence limits, ±3.1%; P = 0.013) and reduced overall tiredness during
sprints by 13% (90% confidence limits, ±9.2%). Serum creatine kinase was
19% (90% confidence limits, ±18%) lower than control, but difference in
lactate dehydrogenase and muscle pain were trivial and unclear. In the
second study, protein-carbohydrate feeding led to moderate and very large
increases in cell signalling to translation; mTOR, 4E-BP1 and RPS6
phosphorylation by 3-h. Bioinformatics analysis indicates protein ingestion
iii
effects the transcriptome response involved in immune/inflammatory
processes, tissue development (extracellular matrix, cytoskeletal, and
scarcomere remodelling), and metabolism consistent with increased fatty
acid oxidation, compared to control.
Post-exercise protein and carbohydrate coingestion during a period of hard
training enhances subsequent high-intensity endurance performance and
may reduce membrane disruption in comparison to high-carbohydrate
feeding. Furthermore, the mechanism responsible for protein-nutrition
mediated adaptation may be through enhancing protein translation and fine-
tuning the gene expression profile induced by exercise.
iv
ACKNOWLEDGEMENTS First I would like to thank Dr David Rowlands, for guidance, support,
motivation, and the huge amount of energy you contribute to anything you
are involved in.
To my secondary supervisors, Assoc. Prof. Welma Stonehouse and Dr Ajmol
Ali, I appreciate your help and guidance with my writing. To Welma, thanks
also for being so approachable and for providing emotional support when
needed.
To my collaborators, Brian Timmons, Frederic Raymond, Andreas Fuerholz,
Robert Mansourian, Marie-Camille Zawhlen, Sylviane Metairon, Elisa Glover,
Trent Stellingwerff, Martin Krussman, and Mark Tarnopolsky thank you for
your help
Thanks to the various lab staff of whom I spent a large portion of my time
with, and especially the following technicians and students; Holly, Amy,
Dave, Simon, Carlos, Helen, Andy, Andre, and Dave G for your help and
friendship.
Thanks also to Dr Andrew Foskett for phlebotomy assistance, Dr Beatrix
Jones for statistical assistance.
Thanks once again to my subjects, who volunteered so much time and effort,
and still came out smiling at the end of it all.
Finally, to my husband Paul, thank you my love for giving me so much
emotional and financial support, and for never doubting me.
v
STATEMENT OF CONTRIBUTION CHAPTER 3: Leucine-protein supplemented recovery feeding
enhances subsequent cycling performance in well-trained men
The principal investigator of this study was Jasmine Thomson. Study
conception and design were provided by Jasmine Thomson, Dr. David
Rowlands, with contributions from Dr. Ajmol Ali. The ethics proposal was
written by Jasmine Thomson. Subjects were recruited and the study was
coordinated by Jasmine Thomson. The supplements were formulated and
prepared by Jasmine Thomson in the Institute of Food, Nutrition and Human
Health Food Technology Laboratories, Massey University, Auckland. The
data was collected largely by Jasmine Thomson with help from Dr. Ajmol Ali,
Dr. Andrew Foskett, with assistance from Simon Bennett. Blood preparation
was done by Jasmine Thomson assisted by Simon Bennett, and analyzed for
Creatine Kinase and Lactate Dehydrogenase through LabPlus. Urine and
sweat samples were collected and prepared by Jasmine Thomson, Kjeldahl
digests and nitrogen determination by distillation and titration performed by
Jasmine Thomson. Serum amino acids were analysed by HPLC at research
laboratory at McMaster University by Tracey Rerecich. Statistical analyses
were performed by Jasmine Thomson with guidance from Dr David
Rowlands and Dr Beatrix Jones. The manuscript was written and prepared
by Jasmine Thomson with guidance from Dr. David Rowlands, Dr. Ajmol Ali,
and Assoc. Prof. Welma Stonehouse.
CHAPTER 4: Increased specificity of immune response, myocyte
remodelling, and metabolic gene expression and signal ling to
translation with protein feeding after prolonged exercise
Study conception and design were provided by Dr. David Rowlands, Dr.
Mark Tarnopolsky and Jasmine Thomson. The study was performed within
the Departments of Medical Science and Pediatrics and Medicine, McMaster
University research laboratories under supervision of Dr. Mark Tarnopolsky.
Subjects were recruited by Jasmine Thomson. The supplements were
prepared by Stuart Lowther of Life Science Nutritionals Inc. Biological
vi
samples were collected by Dr. Mark Tarnopolsky, Dr. David Rowlands, Dr.
Brian Timmons and Jasmine Thomson. Samples were prepared by Holly
Robertshaw, Ming-Hua Fu, Changhua Ye, Michaela Devries, David
Rowlands and Jasmine Thomson. Insulin assay performed by Suzanne
Southward, and glucose by Tracy Rerecich. RNA extraction was done by
Holly Robertshaw assisted by Jasmine Thomson. Western blotting was
performed by by Elisa Glover, and real-time RT-PCR by Holly Robertshaw,
and Changhua Ye. Micro array analysis was done at the Nestle Research
Centre, Vers-chez-les-Blanc, Lausanne, Switzerland. Data Analyses were
performed by Dr. David Rowlands, Jasmine Thomson and Brian Timmons,
apart from the Array data which was performed Frederic Raymond, Robert
Mansourian, Sylviane Metairon, Andreas Fuerholz, and Elisa Glover.
Bioinformatics was by Andreas Fuerholz, David Rowlands, and Frederic
Raymond. The manuscript was written and prepared by Jasmine Thomson
with guidance from Dr. David Rowlands, and contributions from Frederic
Raymond (Illumina array methods) and Andreas Fuerholz (bioinformatics).
The studies were funded by Massey University Research Fund, Sport and
Recreation New Zealand, Life Science Nutritional (Canada), and Nestec
(Switzerland).
vii
RESEARCH ETHICS Ethical approval was obtained from the applicable research ethics bodies for
each study (Massey University Palmerston North Ethics Committee; and
Hamilton Health Sciences/McMaster University, Hamilton, Ontario). The
potential risks and management of risks involved is detailed below;
All participants were screened via a health questionnaire for pre-existing
conditions to ensure they were physically healthy and able to take part in the
studies. Participants were limited to athletes in regular training, and
individuals who were neither disabled nor elderly and at increased risk of
injury or discomfort during the exercise and performance portions of the
research. Some fatigue during exercise and performance trials was to be
expected, however this expected to be of a similar level to that normally
experienced in participant’s own endurance training and competition.
Maximal effort was requested of participants in both the VO2max and
performance testing and associated discomfort was thought to be normal for
this level of athlete, and in fact adaptive and beneficial to health. There may
have been some discomfort and minor risk of infection associated with blood
catheter insertion and muscle biopsy procedures. Discomfort in each
instance was minimised by having subjects lie prone on a hospital bed, and
blood and biopsy procedures were performed by trained phlebotomists and
medics with experience in the procedures. It was considered that the amount
of blood and muscle tissue samples taken to pose no risk of adverse health
effects. Risk of infection was minimised by following sterile procedural
guidelines.
Social and psychological risks were minimised by ensuring privacy and
confidentiality of participants throughout data collection and data storage
periods. Initially we obtained informed consent and communicated to
participants their rights to discontinue or withdraw from the studies at any
time. We also ensured there were adequate change and shower facilities,
and we minimised the number of observers in the laboratory at any one time
while subjects were being examined and tests conducted. Following data
viii
collection and identifying information has been stored securely in locked filing
cabinet in locked office with access to only those principally involved in the
studies.
We aimed to reduce economic risk to participants by reimbursing them for
travel and time where necessary.
ix
TABLE OF CONTENTS CHAPTER 1 INTRODUCTION .............................................................................. 1
1.1.1 PURPOSE OF THESIS ......................................................................... 8
CHAPTER 2 LITERATURE REVIEW ................................................................. 10
2.1 EFFECTS OF POST-EXERCISE PROTEIN-CARBOHYDRATE CO-
INGESTION ON SUBSEQUENT ENDURANCE EXERCISE PERFORMANCE
AND CANDIDATE MECHANISMS ................................................................... 10
2.1.1 ABSTRACT ......................................................................................... 10
2.1.2 BACKGROUND ................................................................................. 11
2.1.3 METHODS .......................................................................................... 13
2.1.4 SHORT-TERM RECOVERY STUDIES (<8 h recovery period) ....... 15
2.1.5 LONGER-TERM RECOVERY STUDIES (>8 h recovery period) .... 35
2.1.6 CONCLUSION AND DIRECTIONS FOR FURTHER RESEARCH 49
CHAPTER 3 STUDY 1 .......................................................................................... 51
3.1 LEUCINE-PROTEIN SUPPLEMENTED RECOVERY FEEDING
ENHANCES SUBSEQUENT CYCLING PERFORMANCE IN WELL-
TRAINED MEN .................................................................................................... 52
3.1.1 ABSTRACT ......................................................................................... 53
3.1.2 INTRODUCTION ............................................................................... 54
3.1.3 MATERIALS AND METHODS ......................................................... 56
3.1.4 RESULTS ............................................................................................ 67
3.1.5 DISCUSSION ...................................................................................... 74
3.1.6 ACKNOWLEDGMENTS ................................................................... 80
x
3.1.7 GRANTS.............................................................................................. 80
CHAPTER 4 STUDY 2.......................................................................................... 81
4.1 TRANSCRIPTOME AND TRANSLATIONAL SIGNALING
FOLLOWING ENDURANCE EXERCISE IN TRAINED SKELETAL
MUSCLE: IMPACT OF DIETARY PROTEIN.................................................... 82
4.1.1 ABSTRACT ......................................................................................... 83
4.1.2 INTRODUCTION ............................................................................... 84
4.1.3 MATERIALS AND METHODS ......................................................... 87
4.1.4 RESULTS .......................................................................................... 100
4.1.5 DISCUSSION .................................................................................... 125
4.1.6 Summary ............................................................................................ 137
4.1.7 Supplementary Information ............................................................... 138
CHAPTER 5 GENERAL DISCUSSION ............................................................. 141
5.1.1 INTRODUCTION ............................................................................. 141
5.1.2 PERFORMANCE OUTCOME ......................................................... 143
5.1.3 MECHANISMS FOR DELAYED PERFORMANCE BENEFIT .... 145
5.1.4 CONCLUSION .................................................................................. 157
5.1.5 DELIMITATIONS ............................................................................ 158
5.1.6 LIMITATIONS .................................................................................. 159
5.1.7 RECOMMENDATIONS FOR FUTURE RESEARCH .................... 160
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LIST OF TABLES TABLE 2.1 EFFECT OF COMBINED PROTEIN-CARBOHYDRATE POST-
EXERCISE FEEDING ON SERUM INSULIN (< 8 h recovery period) ............ 17
TABLE 2.2 EFFECT OF COMBINED PROTEIN-CARBOHYDRATE POST-
EXERCISE FEEDING ON MUSCLE GLYCOGEN (>8 h recovery period) .... 26
TABLE 2.3 EFFECT OF ACUTE COMBINED PROTEIN-CARBOHYDRATE
POST-EXERCISE FEEDING ON SHORT-TERM (<8 h) RECOVERY OF
SUBSEQUENT PERFORMANCE ........................................................................ 32
TABLE 2.4 EFFECT OF ACUTE COMBINED PROTEIN-CARBOHYDRATE
POST-EXERCISE FEEDING ON LONGER-TERM (> 8h) RECOVERY OF
SUBSEQUENT PERFORMANCE ........................................................................ 41
TABLE 3.1 COMPOSITION OF POST-EXERCISE SUPPLEMENT
BEVERAGE AND ACCOMPANYING RECOVERY FOOD .............................. 63
TABLE 3.2 EFFECT OF POST-EXERCISE SUPPLEMENTATION
CONDITION ON ENZYME MARKERS OF MUSCLE MEMBRANE
DISRUPTION DURING THE 4 d BLOCK ............................................................ 71
TABLE 3.3 NITROGEN BALANCE SUMMARY OVER THE 4 d BLOCK ...... 72
TABLE 4.1 SUMMARY OF GENE SELECTION .............................................. 101
TABLE 4.2 WHOLE-BODY PROTEIN TURNOVER OVER THE RECOVERY
PERIOD 22 h FOLLOWING EXERCISE ........................................................... 123
xii
LIST OF FIGURES Figure 2.1 Simplified schematic diagram showing insulin regulation of glucose
uptake and muscle glycogen synthesis. ..................................................................... 23
Figure 2.2 Hypothesized regulation of transcript initiaition and elongation induced
by post-exercise ingestion of protein and carbohydrate combined. ........................... 45
Figure 2.3 Hypothesized transcript and protein accumulation resulting in phenotype
change with successive bouts of endurance exercise ................................................. 48
Figure 3.1 Experimental design ................................................................................. 58
Figure 3.2 Plasma leucine, essential and total amino-acid concentrations following
exercise and for 120-min after ingestion of the leucine-protein and control
supplements................................................................................................................ 68
Figure 3.3 Effect of the leucine-protein supplement on sprint mean power during the
performance test ......................................................................................................... 70
Figure 3.4 The effect of treatment on mood state. ..................................................... 74
Figure 4.1 Experimental design ................................................................................. 87
Figure 4.2 Summary of the molecular programme and affected biological processes
initiated by the addition of protein to high carbohydrate-lipid nutrition following
high-intensity endurance exercise ............................................................................ 104
Figure 4.3 Top IPA networks for ontology families developmental processes, muscle
contraction, and immunity and defence responding to the differential effect of PTN
at 3 h and 48 h .......................................................................................................... 117
Figure 4.4 Effect of the addition of protein to high carbohydrate-lipid nutrition
following high-intensity endurance exercise on the phosphorylation of proteins
regulating mTORC1 and downstream translation initiation .................................... 122
Figure 4.5 Effect of the addition of protein to high carbohydrate-lipid nutrition
following high-intensity endurance exercise on plasma insulin and glucose, muscle
glycogen, and Z-disk streaming ............................................................................... 124
xiii
ABBREVIATIONS AND ACRONYMS 4EBP1 Eukaryotic initiation factor 4E binding protein 1
AA Amino acid
AADACL2 Aralkylamine N-acetyltransferase
AANAT Aralkylamine N-acetyltransferase
ACOX1 Acyl-CoA oxidase 1, palmitoyl
ACSL1 Acyl-CoA synthetase long-chain family member 1
ACTA2 Actin, alpha 2, smooth muscle, aorta
ACTC1 Actin, alpha, cardiac muscle 1
ADCYAP1 Adenylate cyclase activating polypeptide 1 (pituitary)
ADD Adducin
ADORA2A Adenosine A2a receptor
ADP Adenosine diphosphate
AEBSF Aprotinin, Leupeptin, Bestatin, Pepstatin
AKT Protein kinase B
AKT1 AKT substrate 1 (proline-rich)
AMP Adenosine monophosphate
AMPK Adenosine monophosphate kinase
ANGPT2 Angiopoietin 2
ANOVA Analysis of variance
AS3MT Arsenic (+3 oxidation state) methyltransferase
ATP Adenosine triphosphate
B2M Beta 2 microglobulin
BCL2 B-cell CLL/lymphoma 2
BCL2L14 BCL2-like 14 (apoptosis facilitator)
BCOADK Branched-chain 2- oxo-acid dehydrogenase kinase
BDNF Brain-derived neurotrophic factor
C1QA Complement component 1, q subcomponent, A chain
C1QB Complement component 1, q subcomponent, B chain
C1QC Complement component 1, q subcomponent, C chain
C1S Complement component 1, s subcomponent
C21orf127 Chromosome 21 open reading frame 127
CABP5 Calcium binding protein 5
CALML5 Calmodulin-like 5
CaMK Calcium/calmodulin-dependent protein kinase II
xiv
CAMKID Calcium/calmodulin-dependent protein kinase ID
CAMKII Calcium/calmodulin-dependent protein kinase II
CASP1 Caspase 1, apoptosis-related cysteine peptidase (interleukin 1,
beta, convertase)
CASP10 Caspase 10, apoptosis-related cysteine peptidase
CASP3 Caspase 3, apoptosis-related cysteine peptidase
CCL22 Chemokine (C-C motif) ligand 22
CCL5 Chemokine (C-C motif) ligand 5
CD36 Cluster of Differentiation 36
CD86 CD86 molecule
cDNA Complimentary deoxyribonucleic acid
CEBPB CCAAT/enhancer binding protein (C/EBP), beta
cFOS FOS proto-oncogene
CHAT Choline O-acetyltransferase
CHO Carbohydrate
CI Confidence interval
CIB2 Calcium and integrin binding family member 2
cJUN JUN proto-oncogene
CK Creatine kinase
CL Confidence limit
CLCN4 Chloride channel protein 4
COL10A1 Collagen, type X, alpha 1
COL11A2 Collagen, type XI, alpha 2
COL18A1 Collagen, type XVIII, alpha 1
COL1A1 Collagen, type I, alpha 1
COL1A2 Collagen, type I, alpha 2
COL22A1 Collagen, type XXII, alpha 1
COL3A1 Collagen, type III, alpha 1
COL5A1 Collagen, type V, alpha 1
COL5A2 Collagen, type V, alpha 2
COL6A1 Collagen, type VI, alpha 1
COL6A3 Collagen, type VI, alpha 3
COLQ Collagen-like tail subunit (single strand of homotrimer) of
asymmetric acetyl cholinesterase
CON Control condition
xv
CPS1 Carbamoyl-phosphate synthase 1, mitochondrial
CPT1 Carnitine palmitoyltransferase I
CPT2 Carnitine palmitoyltransferase 2
CREB cAMP response element binding protein
cRNA Complementary ribonucleic acid
CROT Carnitine O-octanoyltransferase
CT Cycle threshold
CTSC Cathepsin C
CV Coefficient of variation
CXCL12 Chemokine (C-X-C motif) ligand 12
CXCL2 Chemokine (C-X-C motif) ligand 2
CXCR4 Chemokine (C-X-C motif) receptor 4
CYCS Cytochrome c, somatic
CYP2U1 Cytochrome P450, family 2, subfamily U, polypeptide 1
CYP46A1 Cytochrome P450, family 46, subfamily A, polypeptide 1
d 15N dose
DDIT3 DNA-damage-inducible transcript 3 (C/EBP-homologous protein,
CHOP, GADD153)
DEPC Diethylpyrocarbonate
DLAT Dihydrolipoamide S-acetyltransferase
DMD Dystrophin
DNA Deoxyribonucleic acid
DNAJ 40 kDa heat shock protein (HSP40)
Dnase Deoxyribonuclease
DNMT3 DNA (cytosine-5-)-methyltransferase 3 alpha
DNMT3B DNA (cytosine-5-)-methyltransferase 3 beta
DSCR1 Regulator of calcineurin 1 (RCAN1, MCIP1)
DTT Glucose assay buffer
EAA Essential amino acids
ECH1 Enoyl CoA hydratase 1, peroxisomal
ECM Extracellular matrix
EDN1 Endothelin 1
EDTA Ethylenediaminetetraacetic acid
EE Estimated energy expenditure
EE1A1 Eukaryotic translation elongation factor 1 alpha 1
xvi
EFEMP1 EGF-containing fibulin-like extracellular matrix protein 1
EFNB1 Ephrin-B1
EFNB3 EPH receptor B3
EGF Epidermal growth factor
EGTA Ethylene glycol tetra acetic acid
EIF1AX Eukaryotic translation initiation factor 1A, X-linked
eIF2B Eukaryotic translation initiation factor 2B
eIF4E Eukaryotic translation initiation factor 4E
eIF4G Eukaryotic translation initiation factor 4G
EIF5B Eukaryotic translation initiation factor 5B
ELISA Enzyme-Linked Immunosorbent Assay, enzyme immunoassay
eNOS Endothelial nitric oxide synthase 3 (endothelial cell)
EPHA2 EPH receptor A2
ERK 1/2 Mitogen-activated protein kinase
ES Effect Size
ESR1 Estrogen receptor 1
Exstudy Estimated energy expenditure for study exercise protocol
FABP3 Fatty acid binding protein 3
FABP5 Fatty acid binding protein 5
FAK Focal adhesion kinase
FBLN1 Fibulin 1
FBLN2 Fibulin 2
FBXL3 F-box and leucine-rich repeat protein 3
FBXO24 F-box protein 24
FBXO32 F-box protein 32
FGF2 Fibroblast growth factor 2
FOXO1a Forkhead box O1
FOXO3 Forkhead box O3
G6PDH Glucose-6-phosphate dehydrogenase
GADD45B Growth arrest and DNA-damage-inducible, beta
GAPDH Glyceraldehyde-3-phosphate dehydrogenase
GCN5 General control of amino-acid synthesis 5-like 2
GDF1 Growth differentiation factor 1
GDF8 Myostatin
GEA Global Error Assessment
xvii
GLUT4 Glucose transporter type 4
GRS Graphic rating scale
GSK3 Glycogen synthase
G L G-protein beta-subunit like protein
HAT1 Histone acetyltransferase 1
HCHO High carbohydrate condition
HDAC8 Histone deacetylase 8
HEPES 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer
HGF Hepatocyte growth factor
HMGCS2 3-hydroxy-3-methylglutaryl-CoA synthase 2 (mitochondrial)
HSP70 Heat shock 70 kDa protein 1A (HSPA1A)
HSPA1A Heat shock 70 kDa protein 1A (HSP70)
hVPS34 Phosphatidylinositol 3-kinase catalytic subunit type 4
ICMT Isoprenylcysteine carboxyl methyltransferase
IFI6 Interferon, alpha-inducible protein 6
IFITM2 Interferon induced transmembrane protein 2 (1-8D)
IFNA1 Interferon, alpha 1
IGF1 Insulin-like growth factor 1
IKBKB Inhibitor of kappa light polypeptide gene enhancer in B-cells,
kinase beta
IL Interleukin
IL17D Interleukin 17D
IL1F6 Interleukin 1 family, member 6
IL1F8 Interleukin 1 family, member 8
IL22 Interleukin 22
IPA Ingenuity pathway analysis
IRF8 Interferon regulatory factor 8
IRS1 Insulin receptor substrate 1
ITGAM Integrin, alpha M (complement component 3 receptor 3 subunit)
ITGB1 Integrin, beta 1
ITGB2 Integrin, beta 2
JNK c-Jun N-terminal kinases
LAMA4 Laminin, alpha 4
LCHO Low carbohydrate condition
LDH Lactate Dehydrogenase
xviii
LPIN1 Lipin 1
LPL Lipoprotein lipase
LRFN5 Leucine rich repeat and fibronectin type III domain containing 5
MAPK Mitogen-activated protein kinase
MDA Malonyldialdehyde
MEF2 Myocyte enhancer factor 2
MG Macro-glycogen
MHC Myosin heavy chain
MHCII Major Histocompatibility Complex class II
MLC1SA Myosin, light chain 6B, alkali, smooth muscle and non-muscle
(MYL6B)
MMP13 Matrix metallopeptidase 13 (collagenase 3)
MMP19 Matrix metallopeptidase 19
MMP9 Matrix metallopeptidase 9 (92 kDa gelatinase, type IV
collagenase)
MRCL3 Myosin, light chain 12A, regulatory, non-sarcomeric1 (MYL12A)
MRF4 Myogenic factor 6 (also known as Muscle-specific regulatory
factor 4)
MRFAP1L1 Morf4 family associated protein 1-like 1
mRNA Messenger ribonucleic acid
MTMR6 Myotubularin related protein 6
mTOR Mammalian target of rapamycin
mTORC1 Mammalian target of rapamycin complex 1
MUC4 Mucin 4, cell surface associated
MuRF1 Muscle-specific RING finger protein 1
MYBPH Myosin binding protein H
MYF5 Myogenic factor 5
MYH1 Myosin, heavy chain 1, skeletal muscle, adult
MYH8 Myosin, heavy chain 8, skeletal muscle, perinatal
MYL1 Myosin, light chain 1, alkali; skeletal, fast
MYL2 Myosin, light chain 2, regulatory, cardiac, slow
MYL3 Myosin, light chain 3, alkali; ventricular, skeletal, slow
MYL4 Myosin, light chain 4, alkali; atrial, embryonic
MYL5 Myosin, light chain 5, regulatory
MYLPF Myosin light chain, phosphorylatable, fast skeletal muscle
xix
MYOD1 Myogenic differentiation 1
MYOG Myogenin (myogenic factor 4)
MYST2 MYST histone acetyltransferase 2
n Sample number
NADP Nicotinamide adenine dinucleotide phosphate
NCBI GEO Gene expression omnibus
NDST2 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2
NE Nitrogen excretion
NES Mestin
NFAT Nuclear factor of activated T-cells
NF-kB Nuclear factor-kB
NFKB1A Nuclear factor of kappa light polypeptide gene enhancer in B-
cells 1
NI Nitrogen intake
NKIRAS2 Nuclear factor of kappa light polypeptide inhibitor interacting Ras-
like 2
NMR Nuclear magnetic resonance spectroscopy
NPB Net protein balance
NTN4 Metrin 4
NTNG2 Metrin G2
p Test statistic probability considered significant at the a-level 0.05
p70S6K Ribosomal protein S6 kinase, 70 kDa
p90RSK Ribosomal protein S6 kinase, 90 kDa
PA Physical Activity
Panther GO Panther gene ontology mapping
PB Protein breakdown
PCR Polymerase chain reaction
PDE Phosphodiesterase
PDGFB Platelet-derived growth factor beta polypeptide
PDHA2 Pyruvate dehydrogenase (lipoamide) alpha 2
PDK Pyruvate dehydrogenase kinase
PDK1 Phosphinositide dependent protein kinase 1
PDZRN3 PDZ domain containing ring finger 3
PECI Peroxisomal D3,D2-enoyl-CoA isomerase
PFKFB1 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1
xx
PFKFB3 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3
PFKM Phosphofructokinase, muscle
PG Pro-glycogen
PGC-1 PPAR gamma coactivator 1 alpha
PH Plekstrin homology domain containing proteins
PI3K Phosphinositide 3-kinase
PIK3CA Phosphoinositide-3-kinase, catalytic, alpha polypeptide
PKC Protein kinase C
PLA2 Phospholipase A2
PLIN2 Perilipin 2
PLTP Phospholipid transfer protein
POMS Profile of mood states short-form questionnaire
PPAR Peroxisome proliferator-activated receptor
PPAR Peroxisome proliferator-activated receptor gamma
PPARGC1 Peroxisome proliferator-activated receptor gamma, coactivator 1
alpha
PPM2C Pyruvate dehydrogenase phosphatase catalytic subunit 1 (PDP1)
PRAS40 40 kDa proline-rich AKT substrate
PS Protein synthesis
PTN, Ptn Protein condition
Q Nitrogen flux
qPCR Real time reverse transcription polymerase chain reaction
r Pearson's correlation (one-tailed)
Rab 7 GTPase Rab 7
Rag A/B/C/D Ras-related GTP-binding proteins
RARA Retinoic acid receptor, alpha
REDD1/2 Deoxyribonucleic acid-damage-inducible transcript 4
RFFL Ring finger and FYVE-like domain containing 1
RHEB Ras homolog enriched in brain
RHOA Ras homolog gene family, member A
RHOC Ras homolog gene family, member C
RHOJ Ras homolog gene family, member J
RMR Resting metabolic rate
RNA Ribonucleic acid
RNAase Ribonuclease
xxi
ROS Reactive oxygen species
RPE Ratings of perceived exertion
RPL27A Ribosomal protein L27a
RPL7 Ribosomal protein L7
RPLP0 Ribosomal protein, large, P0
RPLP1 Ribosomal protein, large, P1
RPS6 40S ribosomal protein S6
RPS6KA1 Ribosomal protein S6 kinase, 90 kDa, polypeptide 1
rRNA Ribosomal ribonucleic acid
RSP24 Ribosomal protein S24
RSP3A Ribosomal protein S3a
RT Reverse transcription
RT-PCR Real time reverse transcription polymerase chain reaction
S100A8 S100 calcium binding protein A8
S100A9 S100 calcium binding protein A9
S6K Ribosomal protein S6 kinase, 70 kDa (formerly known as
p70S6K)
SAS Statistical Analysis Software
SCD Stearoyl-CoA desaturase (delta-9-desaturase)
SD Standard deviation
SDC2 Syndecan 2
SDF1 Chemokine (C-X-C motif) ligand 12 (CXCL12)
SDS PAGE Sodium dodecyl sulphate polyacrylamide gel electrophoresis
SEMA3C Sema domain, immunoglobulin domain, short basic domain,
secreted, (semaphorin) 3C
SEMA3F Sema domain, immunoglobulin domain, short basic domain,
secreted, (semaphorin) 3F
SEMA6A Sema domain, transmembrane domain, and cytoplasmic domain,
(semaphorin) 6A
Ser Serine rich binding motif
SERCA Sarco/endoplasmic reticulum calcium transporting ATPase
SIRT5 Sirtuin 5
SIRT6 Sirtuin 6
SLC1A5 Neutral amino acid transporter solute carrier family 1
SLC25A20 Solute carrier family 25 (carnitine/acylcarnitine translocase),
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member 20
SLC2A4 Solute carrier family 2 (facilitated glucose transporter), member 4
(GLUT4)
SLC7A11 Solute carrier family 7, (cationic amino acid transporter, y+
system) member 11
SLC7A5 Solute carrier family 7 (cationic amino acid transporter, y+
system), member 5
SLC7A5/SLC3A2 Bi-directional antiporter
SLC7A8 Solute carrier family 7 (amino acid transporter, L-type), member 8
SLCO1B1 Solute carrier organic anion transporter family, member 1B1
SLCO2A1 Solute carrier organic anion transporter family, member 2A1
SLIT2 Slit homolog 2
SMAD3 SMAD family member 3
SMARCA3 Helicase-like transcription factor (HLTF)
SNP sites Single nucleotide polymorphism or single nucleotide (A, T, C, or
G) difference
SOCS3 Suppressor of cytokine signalling 3
SOD Superoxide dismutase
SPSS Statistical Package for the Social Sciences
SR Sarcoplasmic reticulum
SREBP Sterol response element binding protein
SULT1A1 Sulfotransferase family, cytosolic, 1A, phenol-preferring, member
1
SYK Spleen tyrosine kinase
TBK1 TANK-binding kinase 1
TBS-T Tris buffered saline solution with the detergent Tween-20
TGFB1 Transforming growth factor, beta 1
Thr Threonine rich binding motif
TIMP1 TIMP metallopeptidase inhibitor 1
TIMP2 TIMP metallopeptidase inhibitor 2
TLR3 Toll-like receptor 3
TNC Tenascin C
TNF Tumour necrosis factor
TNFRSF19 Tumour necrosis factor receptor super family, member 19
TNFSF11 Tumour necrosis factor (ligand) super family, member 11
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TNN Tenascin N
TNNT2 Troponin T type 2 (cardiac)
TNXB Tenascin XB
tr:T Tracer to tracee ratio
TRIM46 Tripartite motif-containing 46
TRIM5 Tripartite motif-containing 5
TRIM9 Tripartite motif-containing 9
Tris Tris(hydroxymethyl)aminomethane buffer
TSC1 Tuberous sclerosis protein 1, (hamartin)
TSC1-TSC2 Hamartin-tuberin complex
TSC2 Tuberous sclerosis protein 2 (tuberin)
TUBA1 Tubulin alpha-1A chain
Tween Polysorbate detergent
Tyr Tyrosine rich binding motif
UBE2 Ubiquitin-conjugating enzyme E2
UBE2J2 Ubiquitin-conjugating enzyme E2, J2
UCP3 Uncoupling protein 3 (mitochondrial, proton carrier)
VEGF Vascular endothelial growth factor
VEGFA Vascular endothelial growth factor A
VIM Vimentin
VO2max Maximal volume of oxygen consumed
Vsp15 Vacuole sorting protein 15
Wmax Peak power output
WNT5A Wingless-type MMTV integration site family, member 5A
YY1 YY1 transcription factor
ZNRF2 Zinc and ring finger 2